ID PRXC_STRAU Reviewed; 278 AA. AC O31168; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 16-JUN-2009, entry version 59. DE RecName: Full=Non-heme chloroperoxidase; DE EC=1.11.1.10; DE AltName: Full=Chloride peroxidase; DE AltName: Full=Chloroperoxidase T; DE Short=CPO-T; GN Name=cpo; Synonyms=cpoT; OS Streptomyces aureofaciens. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1894; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Tu24; RA Pelletier I., Altenbuchner J., van Pee K.-H.; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS). RC STRAIN=Tu24; RX MEDLINE=98307994; PubMed=9642069; DOI=10.1006/jmbi.1998.1802; RA Hofmann B., Tolzer S., Pelletier I., Altenbuchner J., van Pee K.-H., RA Hecht H.-J.; RT "Structural investigation of the cofactor-free chloroperoxidases."; RL J. Mol. Biol. 279:889-900(1998). CC -!- CATALYTIC ACTIVITY: RH + Cl(-) + H(2)O(2) = RCl + 2 H(2)O. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the bacterial non-heme bromo- and chloro- CC peroxidases family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF031242; AAB86626.1; -; Genomic_DNA. DR PDB; 1A7U; X-ray; 1.75 A; A/B=2-278. DR PDB; 1A8U; X-ray; 1.60 A; A/B=2-278. DR PDBsum; 1A7U; -. DR PDBsum; 1A8U; -. DR MEROPS; S33.991; -. DR PeroxiBase; 5908; STaHalNPrx02. DR BRENDA; 1.11.1.10; 2126. DR GO; GO:0031404; F:chloride ion binding; IEA:UniProtKB-KW. DR GO; GO:0016691; F:chloride peroxidase activity; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR000073; AB_hydrolase_1. DR Pfam; PF00561; Abhydrolase_1; 1. PE 1: Evidence at protein level; KW 3D-structure; Chloride; Oxidoreductase; Peroxidase. FT CHAIN 1 278 Non-heme chloroperoxidase. FT /FTId=PRO_0000207062. FT ACT_SITE 99 99 By similarity. FT ACT_SITE 229 229 By similarity. FT ACT_SITE 258 258 By similarity. FT STRAND 3 9 FT STRAND 12 30 FT HELIX 37 40 FT HELIX 41 49 FT STRAND 53 57 FT HELIX 74 88 FT STRAND 92 98 FT HELIX 101 112 FT STRAND 117 124 FT STRAND 139 141 FT HELIX 143 155 FT HELIX 157 168 FT HELIX 171 174 FT TURN 176 178 FT HELIX 181 193 FT HELIX 196 205 FT TURN 211 213 FT HELIX 214 216 FT STRAND 221 226 FT STRAND 230 232 FT HELIX 234 236 FT HELIX 238 244 FT STRAND 248 253 FT HELIX 260 263 FT HELIX 265 277 SQ SEQUENCE 278 AA; 30355 MW; 8C97A87251FBEDE5 CRC64; MPFITVGQEN STSIDLYYED HGAGQPVVLI HGFPLSGHSW ERQSAALLDA GYRVITYDRR GFGQSSQPTT GYDYDTFAAD LNTVLETLDL QDAVLVGFSM GTGEVARYVS SYGTARIAKV AFLASLEPFL LKTDDNPDGA APKEFFDGIV AAVKADRYAF YTGFFNDFYN LDENLGTRIS EEAVRNSWNT AASGGFFAAA AAPTTWYTDF RADIPRIDVP ALILHGTGDR TLPIENTARV FHKALPSAEY VEVEGAPHGL LWTHAEEVNT ALLAFLAK //